Receptins: a novel term for an expanding spectrum of natural and engineered microbial proteins with binding properties for mammalian proteins

Abstract

A new term 'receptin', derived from recipere (lat.), is proposed to denote microbial binding proteins that interact with mammalian target proteins. An example of such a 'receptin' is staphyloccocal protein A which binds to the Fc part of many mammalian immunoglobulins. Several other types of 'receptins' are listed. This term may easily be distinguished from the similar term 'receptor', describing a binding site on a cell surface, mostly eukaryotic, where a secondary effect is induced inside the cell upon binding to a ligand. A receptin, however, does not necessarily have to induce a secondary event. Receptins include so called MSCRAMMs, adhesins, and also engineered receptins, affibodies, and engineered ligands. It denotes any protein of microbial origin, cell-bound or soluble, which can bind to a mammalian protein. It fulfills the need for an umbrella terminology for a large group of binding structures. In contrast, the term 'lectin' represents a group of proteins with affinity for carbohydrate structures. The new term 'receptin' includes a number of key microbial proteins involved in host-parasite interactions and in virulence. Some receptins are promising vaccine candidates.

The binding of Tritrichomonas foetus to immobilized laminin-1 and its role in the cytotoxicity exerted by the parasite

“…Different types of LMN-1-binding molecules have been found in micro-organisms and mammalian cells, including LMN-binding proteins (Mercurio, 1995), integrins (Hynes, 2002;Rao et al, 1992; Hernandez-Ramirez et al, 2000) and receptins (Kronvall & Jonsson, 1999). In the present study we were able to identify the chemical nature of T. foetus LMN-binding molecules, and their dependence on divalent cations.…”

The Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens

“…Second, the full-length Eap protein is sensitive to protease treatment and is readily digested into soluble, protease-stable fragments corresponding to individual EAP domains. 3 This suggests that these linker residues are solvent-exposed and/or -accessible. Finally, EAP domains assume a fold where the Nand C-terminal residues are located at the opposite sides of the molecule.…”

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently

“…Although not focused on biocatalysis, other scaffolds such as lipocalins [421][422][423][424][425][426] and affibodies [427][428][429][430][431][432][433][434][435][436][437] have proved useful for combinatorial biosynthesis and directed evolution.…”